HEM11_ARATH
ID HEM11_ARATH Reviewed; 543 AA.
AC P42804; Q0WWL6; Q9LQB9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glutamyl-tRNA reductase 1, chloroplastic;
DE Short=GluTR;
DE EC=1.2.1.70;
DE Flags: Precursor;
GN Name=HEMA1; Synonyms=HEMA; OrderedLocusNames=At1g58290; ORFNames=F19C14.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7908550; DOI=10.2307/3869644;
RA Ilag L.L., Kumar A.M., Soell D.;
RT "Light regulation of chlorophyll biosynthesis at the level of 5-
RT aminolevulinate formation in Arabidopsis.";
RL Plant Cell 6:265-275(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY LIGHT, AND TISSUE SPECIFICITY.
RX PubMed=11309145; DOI=10.1046/j.1365-313x.2001.00986.x;
RA McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.;
RT "Regulation of HEMA1 expression by phytochrome and a plastid signal during
RT de-etiolation in Arabidopsis thaliana.";
RL Plant J. 25:549-561(2001).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=12139011; DOI=10.1023/a:1016081114758;
RA Ujwal M.L., McCormac A.C., Goulding A., Kumar A.M., Soell D., Terry M.J.;
RT "Divergent regulation of the HEMA gene family encoding glutamyl-tRNA
RT reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by
RT sugars, but is independent of light and plastid signalling.";
RL Plant Mol. Biol. 50:83-91(2002).
RN [8]
RP INTERACTION WITH FLU, ACTIVITY REGULATION, AND DOMAIN.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15584960; DOI=10.1111/j.1365-313x.2004.02262.x;
RA Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K.;
RT "Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1),
RT the target of metabolic feedback inhibition of tetrapyrrole biosynthesis,
RT in dark- and light-grown Arabidopsis plants.";
RL Plant J. 40:957-967(2004).
RN [9]
RP INDUCTION BY LIGHT.
RX PubMed=19380736; DOI=10.1073/pnas.0811684106;
RA Stephenson P.G., Fankhauser C., Terry M.J.;
RT "PIF3 is a repressor of chloroplast development.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7654-7659(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GLUTRBP.
RX PubMed=22180625; DOI=10.1105/tpc.111.086421;
RA Czarnecki O., Hedtke B., Melzer M., Rothbart M., Richter A., Schroter Y.,
RA Pfannschmidt T., Grimm B.;
RT "An Arabidopsis GluTR binding protein mediates spatial separation of 5-
RT aminolevulinic acid synthesis in chloroplasts.";
RL Plant Cell 23:4476-4491(2011).
RN [11]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP MEMBRANE COMPLEX, AND ACTIVITY REGULATION.
RX PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT physically linked to the final steps of the Mg(++)-branch of this
RT pathway.";
RL FEBS Lett. 586:211-216(2012).
RN [12]
RP INTERACTION WITH CLPF.
RX PubMed=26419670; DOI=10.1105/tpc.15.00574;
RA Nishimura K., Apitz J., Friso G., Kim J., Ponnala L., Grimm B.,
RA van Wijk K.J.;
RT "Discovery of a unique Clp Component, ClpF, in chloroplasts: A proposed
RT binary ClpF-ClpS1 adaptor complex functions in substrate recognition and
RT delivery.";
RL Plant Cell 27:2677-2691(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 73-543, AND SUBUNIT.
RX PubMed=24753615; DOI=10.1073/pnas.1400166111;
RA Zhao A., Fang Y., Chen X., Zhao S., Dong W., Lin Y., Gong W., Liu L.;
RT "Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with
RT its stimulator protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6630-6635(2014).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). Probably involved in the
CC tetrapyrrole synthesis required for the chlorophyll biosynthesis.
CC {ECO:0000269|PubMed:12139011, ECO:0000269|PubMed:7908550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78520; EC=1.2.1.70;
CC Evidence={ECO:0000269|PubMed:7908550};
CC -!- ACTIVITY REGULATION: Negatively regulated by FLU and heme.
CC {ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:22212719}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts (via C-
CC terminus) with FLU, only in the absence of light. Interacts with
CC GLUTRBP and forms a heterotetramer of two GLUTRBP and two HEMA1
CC subunits. Interacts with CLPF (PubMed:26419670).
CC {ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:22180625,
CC ECO:0000269|PubMed:22212719, ECO:0000269|PubMed:24753615,
CC ECO:0000269|PubMed:26419670}.
CC -!- INTERACTION:
CC P42804; Q940U6: FLU; NbExp=3; IntAct=EBI-2319900, EBI-2319882;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:22180625, ECO:0000269|PubMed:22212719,
CC ECO:0000269|PubMed:7908550}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in photosynthetic tissues.
CC Detected in all tissues tested. {ECO:0000269|PubMed:11309145,
CC ECO:0000269|PubMed:12139011, ECO:0000269|PubMed:7908550}.
CC -!- INDUCTION: Circadian-regulation. Up-regulated by light.
CC {ECO:0000269|PubMed:11309145, ECO:0000269|PubMed:12139011,
CC ECO:0000269|PubMed:19380736, ECO:0000269|PubMed:7908550}.
CC -!- DOMAIN: The N-terminus (65-92) is required for heme inhibition, but not
CC for activity. {ECO:0000269|PubMed:15584960}.
CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC with the formation of a thioester intermediate between enzyme and
CC glutamate, and the concomitant release of tRNA(Glu). The thioester
CC intermediate is finally reduced by direct hydride transfer from NADPH,
CC to form the product GSA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000305}.
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DR EMBL; U03774; AAA19118.1; -; Genomic_DNA.
DR EMBL; AC008051; AAF82258.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33532.1; -; Genomic_DNA.
DR EMBL; AY072223; AAL60044.1; -; mRNA.
DR EMBL; AY096600; AAM20250.1; -; mRNA.
DR EMBL; AK226332; BAE98482.1; -; mRNA.
DR PIR; E96616; E96616.
DR RefSeq; NP_176125.1; NM_104609.4.
DR PDB; 4N7R; X-ray; 2.80 A; A/B=73-543.
DR PDB; 4YVQ; X-ray; 2.40 A; A=440-543.
DR PDB; 5CHE; X-ray; 3.20 A; A/B=73-543.
DR PDB; 5YJL; X-ray; 2.70 A; A/B=73-543.
DR PDBsum; 4N7R; -.
DR PDBsum; 4YVQ; -.
DR PDBsum; 5CHE; -.
DR PDBsum; 5YJL; -.
DR AlphaFoldDB; P42804; -.
DR SMR; P42804; -.
DR BioGRID; 27423; 5.
DR IntAct; P42804; 4.
DR MINT; P42804; -.
DR STRING; 3702.AT1G58290.1; -.
DR PaxDb; P42804; -.
DR PRIDE; P42804; -.
DR ProteomicsDB; 247356; -.
DR EnsemblPlants; AT1G58290.1; AT1G58290.1; AT1G58290.
DR GeneID; 842198; -.
DR Gramene; AT1G58290.1; AT1G58290.1; AT1G58290.
DR KEGG; ath:AT1G58290; -.
DR Araport; AT1G58290; -.
DR TAIR; locus:2016605; AT1G58290.
DR eggNOG; ENOG502QQ1H; Eukaryota.
DR HOGENOM; CLU_035113_2_1_1; -.
DR InParanoid; P42804; -.
DR OMA; FAFKCAA; -.
DR OrthoDB; 571265at2759; -.
DR PhylomeDB; P42804; -.
DR BioCyc; ARA:AT1G58290-MON; -.
DR BioCyc; MetaCyc:AT1G58290-MON; -.
DR BRENDA; 1.2.1.70; 399.
DR UniPathway; UPA00251; UER00316.
DR UniPathway; UPA00668; -.
DR PRO; PR:P42804; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42804; baseline and differential.
DR Genevisible; P42804; AT.
DR GO; GO:0009507; C:chloroplast; TAS:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IPI:TAIR.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; TAS:TAIR.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:TAIR.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.460.30; -; 1.
DR HAMAP; MF_00087; Glu_tRNA_reductase; 1.
DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
DR InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR InterPro; IPR018214; GluRdtase_CS.
DR InterPro; IPR036453; GluRdtase_dimer_dom_sf.
DR InterPro; IPR036343; GluRdtase_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR Pfam; PF00745; GlutR_dimer; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Chloroplast; Membrane; NADP;
KW Oxidoreductase; Plastid; Porphyrin biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 62..543
FT /note="Glutamyl-tRNA reductase 1, chloroplastic"
FT /id="PRO_0000013307"
FT REGION 20..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 143..146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 285..290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT CONFLICT 62
FT /note="E -> V (in Ref. 1; AAA19118)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="K -> N (in Ref. 1; AAA19118)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="K -> L (in Ref. 1; AAA19118)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="V -> G (in Ref. 5; BAE98482)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="Q -> H (in Ref. 1; AAA19118)"
FT /evidence="ECO:0000305"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5YJL"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5CHE"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5CHE"
FT HELIX 230..250
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5CHE"
FT HELIX 255..270
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4N7R"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 417..438
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:4YVQ"
FT HELIX 443..466
FT /evidence="ECO:0007829|PDB:4YVQ"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:4YVQ"
FT HELIX 474..497
FT /evidence="ECO:0007829|PDB:4YVQ"
FT HELIX 509..523
FT /evidence="ECO:0007829|PDB:4YVQ"
SQ SEQUENCE 543 AA; 59515 MW; 04A095FEC96CC014 CRC64;
MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR TRRGLIQKAR
CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI GLSIHTAPVE MREKLAIPEA
EWPRAIAELC GLNHIEEAAV LSTCNRMEIY VLALSQHRGV KEVTEWMSKT SGIPVSEICQ
HRFLLYNKDA TQHIFEVSAG LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI
TVGKRVRTET NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK
GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA SETPLFLKEH
VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN VDDLKEVVAA NKEDRMRKAM
EAQTIITEES TQFEAWRDSL ETVPTIKKLR AYAERIRVAE LEKCMSKMGD DINKKTTRAV
DDLSRGIVNR FLHGPMQHLR CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ
QQK
